Retinal is also known as retinaldehyde. It was originally called retinene,[2] and renamed[3] after it was discovered to be vitamin Aaldehyde.[4][5] Retinal is one of the many forms of vitamin A (the number of which varies from species to species). Retinal is a polyenechromophore, bound to proteins called opsins, and is the chemical basis of animal vision. Retinal allows certain microorganisms to convert light into metabolic energy.

Vertebrate animals ingest retinal directly from meat, or they produce retinal from carotenoids, either from one of two carotenes (α-carotene, β-carotene) or from β-cryptoxanthin, a type of xanthophyll. These carotenoids must be obtained from plants or other photosynthetic organisms. No other carotenoids can be converted by animals to retinal, and some carnivores cannot convert any carotenoids at all. The other main forms of vitamin A, retinol, and a partially active form, retinoic acid, may both be produced from retinal.

Invertebrates such as insects and squid use hydroxylated forms of retinal in their visual systems, which derive from conversion from other xanthophylls.

catalyzed by a beta-carotene 15,15'-monooxygenase[7] or a beta-carotene 15,15'-dioxygenase.[8] Just as carotenoids are the precursors of retinal, retinal is the precursor of the other forms of vitamin A. Retinal is interconvertible with retinol (ROL), the transport and storage form of vitamin A

Vision begins with the photoisomerization of retinal. When the 11-cis-retinalchromophore absorbs a photon it isomerizes from the 11-cis state to the all-trans state. The absorbance spectrum of the chromophore depends on its interactions with the opsin protein to which it is bound; different opsins produce different absorbance spectra.

Opsins are proteins and the retinal-binding visual pigments found in the photoreceptor cells in the retinas of eyes. An opsin is arranged into a bundle of seven transmembrane alpha-helices connected by six loops. In rod cells the opsin molecules are embedded in the membranes of the disks which are entirely inside of the cell. The N-terminus head of the molecule extends into the interior of the disk, and the C-terminus tail extends into the cytoplasm of the cell. In cone cells the disks are defined by the cell's plasma membrane so that the N-terminus head extends outside of the cell. Retinal binds covalently to a lysine on the transmembrane helix nearest the C-terminus of the protein through a Schiff base linkage. Formation of the Schiff base linkage involves removing the oxygen atom from retinal and two hydrogen atoms from the free amino group of lysine, giving H2O. Retinylidene is the divalent group formed by removing the oxygen atom from retinal, and so opsins have been called retinylidene proteins.

Opsins are prototypical G protein-coupled receptors (GPCRs).[13] Bovine rhodopsin, the opsin of the rod cells of cattle, was the first GPCR to have its X-ray structure determined.[14] Bovine rhodopsin contains 348 amino acid residues. The retinal chromophore binds at Lys296.

Although mammals use retinal exclusively as the opsin chromophore, other groups of animals additionally use four chromophores closely related to retinal. These are 3,4-didehydroretinal, (3R)-3-hydroxyretinal, (3S)-3-hydroxyretinal, and (4R)-4-hydroxyretinal. Many fish and amphibians use 3,4-didehydroretinal, also called dehydroretinal. With the exception of the dipteran suborder Cyclorrhapha, the so-called higher flies, all insects examined use the (R)-enantiomer of 3-hydroxyretinal. The (R)-enantiomer is to be expected if 3-hydroxyretinal is produced directly from xanthophyll carotenoids. Cyclorrhaphans, including Drosophila, use (3S)-3-hydroxyretinal.[15][16]Firefly squid have been found to use (4R)-4-hydroxyretinal.

Type 2 rhodopsin (rainbow colored) embedded in a lipid bilayer (heads red and tails blue) with transducin below it. Gtα is colored red, Gtβ blue, and Gtγ yellow. There is a bound GDP molecule in the Gtα-subunit and a bound retinal (black) in the rhodopsin. The N-terminus terminus of rhodopsin is red and the C-terminus blue. Anchoring of transducin to the membrane has been drawn in black.

RPE65 isomerohydrolases are homologous with beta-carotene monooxygenases;[6] the homologous ninaB enzyme in Drosophila has both retinal-forming carotenoid-oxygenase activity and all-trans to 11-cis isomerase activity.[19]

All-trans-retinal is also an essential component of type I, or microbial, opsins such as bacteriorhodopsin, channelrhodopsin, and halorhodopsin. In these molecules, light causes the all-trans-retinal to become 13-cis retinal,[20] which then cycles back to all-trans-retinal in the dark state.